6BZD
Structure of 14-3-3 gamma R57E mutant bound to GlcNAcylated peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-11-23 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 76.366, 60.000, 125.786 |
Unit cell angles | 90.00, 90.50, 90.00 |
Refinement procedure
Resolution | 65.024 - 2.670 |
R-factor | 0.2469 |
Rwork | 0.246 |
R-free | 0.28120 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5USK |
RMSD bond length | 0.005 |
RMSD bond angle | 0.656 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.024 | 2.800 |
High resolution limit [Å] | 2.670 | 2.670 |
Rpim | 0.486 | |
Number of reflections | 31410 | |
<I/σ(I)> | 14.3 | 5.8 |
Completeness [%] | 95.7 | |
Redundancy | 2.5 | |
CC(1/2) | 0.997 | 0.997 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 25% PEG 4000, 0.2 M MgCl2, 0.1 M Tris pH 8.5, 20% glycerol |